Which of the following aspects of catalysis by enzymes can NOT be explained by theFischer Lock and Key Hypothesis?Enzymes will lower the activation energy barrier for reaction.Enzymes will specifically recognize their substrates.Appropriate substrates will bind to the enzyme to form a Michaelis complex.Enzymes have an "active site" where appropriate substrates will be bound.Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.

Enzymes are proteins that catalyze biochemical reactions. Enzymes catalyse the reaction by reducing…

Answered: Which of the following aspects of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Select the graph that correctly illustrates the effect of a positive modifier (effector) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes. The solid blue curve represents the unmodified enzyme. The dashed green curve represents the enzyme in the presence of the effector. R is the highly active form of the enzyme and T is the less active form of the enzyme. Assume that this is a positively cooperative enzyme, meaning that the affinity for substrate increases with increasing substrate concentration.
Some cool enzyme (CE) catalyzes the conversion of compound F to compound A. Which of the following must be true of CE? Choice 1 of 4: CE can facilitate conversion of compound A into compound F. Choice 2 of 4: CE binds more tightly to the substrate F than to the product A. Choice 3 of 4: CE decreases the energy of the transition state between compounds F and A. Choice 4 of 4: CE facilitates net conversion of F to A whenever F is present.
Describe the reactants and products of the following enzyme catalyzed reaction. Names of molecules are sufficient.
The following data was obtained during kinetic analysis of an enzyme with and without an inhibitor. Substrate concentration (mM) Reaction rate without inhibitor (µM/s) Reaction rate with inhibitor (µM/s) 10 28 12 20 50 23 40 83 42 60 107 58 100 139 83 200 179 125 300 197 150 400 209 167 560 227 197 How do you calculate the KM for the enzyme in the absence of an inhibitor. And how do you calculate kcat with the given enzymatic concentration of 5 µM.
Is the dependent variable the reaction time? And what is the controlled variables in this experiment and are there any controls that are used in this experiment?
Carboxypeptidase A, an enzyme that catalyzes hydrolysis of a proteins uses Zn2+. The mineral Zn2+sits in the active site of the Carboxypeptidase A enzyme. The Zn2+ facilitates the reaction of the enzyme and is required to be present for the reaction to occur. Select the best answer. Question 28 options: Zn2+ is an example of allosteric inhibition. Zn2+ is an example of a product. Zn2+ is an example of a noncompetitive inhibitor. Zn2+ is an example of a cofactor Zn2+ is an example of a competitive inhibitor.
On the figure below are shown three Lineweaver-Burk plots for enzyme reactions that have been carried out in the presence, or absence, of an inhibi- tor. Indicate what type of inhibition is predicted based on each Lineweaver- Burk plot. For each plot indicate which line corresponds to the reaction without inhibitor and which line corresponds to the reaction with inhibitor present. 1 1 1 [S] [S] [S]
Enzymes catalyze the rapid formation of product by: lowering the Gibbs free energy of the product raising the Gibbs free energy of the substrate lowering the activation energy between the substrate and the product raising the activation energy between the substrate and the product changing the AG (the change in Gibbs free energy) of the reaction
When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates
Can you explain the following based on its mode of enzyme kinetics: 1) Synthesis/degradation of enzymes 2) Allosteric regulation 3) Covalent modification
Catalysis involves overcoming the activation energy barrier of a reaction. What are three ways by which enzymes can do this?

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